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231225s2018 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.8b01770
|2 doi
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|a pubmed24n0969.xml
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|a (DE-627)NLM290940222
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
1 |
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|a Vogele, Kilian
|e verfasserin
|4 aut
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| 245 |
1 |
0 |
|a Enhanced Efficiency of an Enzyme Cascade on DNA-Activated Silica Surfaces
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|c 2018
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 05.08.2019
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|a Date Revised 05.08.2019
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a In nature, compartmentalized and spatially organized enzyme cascades are utilized to increase the efficiency of enzymatic reactions. From a technologically relevant perspective, synthetic enzyme systems have to be optimized with emphasis on enzyme activity, productivity, scalability, and ease of use. But the underlying principles and relevant parameters that lead to an enhancement of the activity of enzyme cascades through spatial organization are still under debate. Here, we report on the 10-fold activity enhancement of the GOx-HRP enzyme cascade for the oxidation of luminol, when the enzymes are colocalized on micron-scaled solid scaffolds. Both enzymes were initially assembled and concentrated on DNA origami rectangles and finally further concentrated on the surface of silica particles. We show that each particular component of the designed system contributes to the activity enhancement. Furthermore, we measured an influence of the silica particle length scale on the total productivity by a factor of 5-10, but to a lesser extent on the maximum enzyme activity. Our findings demonstrate that micrometer-sized scaffolds can be used to enhance the efficiency of enzyme-cascades by at least a magnitude and that solid-phase scaffolds enable scalability for technological applications
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Enzymes, Immobilized
|2 NLM
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|a Luminol
|2 NLM
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|a 5EXP385Q4F
|2 NLM
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|a Silicon Dioxide
|2 NLM
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|a 7631-86-9
|2 NLM
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|a DNA
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|a 9007-49-2
|2 NLM
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|a Hydrogen Peroxide
|2 NLM
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|a BBX060AN9V
|2 NLM
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|a Glucose Oxidase
|2 NLM
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| 650 |
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|a EC 1.1.3.4
|2 NLM
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| 650 |
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|a Horseradish Peroxidase
|2 NLM
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| 650 |
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|a EC 1.11.1.-
|2 NLM
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| 700 |
1 |
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|a List, Jonathan
|e verfasserin
|4 aut
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|a Simmel, Friedrich C
|e verfasserin
|4 aut
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| 700 |
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|a Pirzer, Tobias
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 34(2018), 49 vom: 11. Dez., Seite 14780-14786
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
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|g volume:34
|g year:2018
|g number:49
|g day:11
|g month:12
|g pages:14780-14786
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|u http://dx.doi.org/10.1021/acs.langmuir.8b01770
|3 Volltext
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